Ask about this productRelated genes to: CASQ2 antibody
- Gene:
- ASPH NIH gene
- Name:
- aspartate beta-hydroxylase
- Previous symbol:
- -
- Synonyms:
- CASQ2BP1, BAH, JCTN, HAAH
- Chromosome:
- 8q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-06-13
- Date modifiied:
- 2016-10-05
- Gene:
- CASQ2 NIH gene
- Name:
- calsequestrin 2
- Previous symbol:
- -
- Synonyms:
- PDIB2
- Chromosome:
- 1p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1992-11-05
- Date modifiied:
- 2019-04-23
Related products to: CASQ2 antibody
Related articles to: CASQ2 antibody
- Catecholaminergic polymorphic ventricular tachycardia is an inherited arrhythmogenic disorder characterized by sudden cardiac death in children. Drug therapy is still insufficient to provide full protection against cardiac arrest, and the use of implantable defibrillators in the pediatric population is limited by side effects. There is therefore a need to explore the curative potential of gene therapy for this disease. We investigated the efficacy and durability of viral gene transfer of the calsequestrin 2 (CASQ2) wild-type gene in a catecholaminergic polymorphic ventricular tachycardia knock-in mouse model carrying the CASQ2(R33Q/R33Q) (R33Q) mutation. - Source: PubMed
Publication date: 2014/06/02
Denegri MarcoBongianino RossanaLodola FrancescoBoncompagni SimonaDe Giusti Verónica CAvelino-Cruz José ELiu NianPersampieri SimoneCurcio AntonioEsposito FrancescaPietrangelo LauraMarty IsabelleVillani LauraMoyaho AlejandroBaiardi PaolaAuricchio AlbertoProtasi FelicianoNapolitano CarloPriori Silvia G - Catecholaminergic polymorphic ventricular tachycardia (CPVT) is an inherited arrhythmogenic disease so far related to mutations in the cardiac ryanodine receptor (RYR2) or the cardiac calsequestrin (CASQ2) genes. Because mutations in RYR2 or in CASQ2 are not retrieved in all CPVT cases, we searched for mutations in the physiological protein partners of RyR2 and CSQ2 in a large cohort of CPVT patients with no detected mutation in these two genes. Based on a candidate gene approach, we focused our investigations on triadin and junctin, two proteins that link RyR2 and CSQ2. Mutations in the triadin (TRDN) and in the junctin (ASPH) genes were searched in a cohort of 97 CPVT patients. We identified three mutations in triadin which cosegregated with the disease on a recessive mode of transmission in two families, but no mutation was found in junctin. Two TRDN mutations, a 4 bp deletion and a nonsense mutation, resulted in premature stop codons; the third mutation, a p.T59R missense mutation, was further studied. Expression of the p.T59R mutant in COS-7 cells resulted in intracellular retention and degradation of the mutant protein. This was confirmed after in vivo expression of the mutant triadin in triadin knock-out mice by viral transduction. In this work, we identified TRDN as a new gene responsible for an autosomal recessive form of CPVT. The mutations identified in the two families lead to the absence of the protein, thereby demonstrating the importance of triadin for the normal function of the cardiac calcium release complex in humans. - Source: PubMed
Publication date: 2012/03/14
Roux-Buisson NathalieCacheux MarineFourest-Lieuvin AnneFauconnier JeremyBrocard JulieDenjoy IsabelleDurand PhilippeGuicheney PascaleKyndt FlorenceLeenhardt AntoineLe Marec HervéLucet VincentMabo PhilippeProbst VincentMonnier NicoleRay Pierre FSantoni ElodieTrémeaux PaulineLacampagne AlainFauré JulienLunardi JoëlMarty Isabelle - Catecholaminergic polymorphic ventricular tachycardia is an inherited disease that predisposes to cardiac arrest and sudden death. The disease is associated with mutations in the genes encoding for the cardiac ryanodine receptor (RyR2) and cardiac calsequestrin (CASQ2). CASQ2 mutations lead to a major loss of CASQ2 monomers, possibly because of enhanced degradation of the mutant protein. The decrease of CASQ2 is associated with a reduction in the levels of Triadin (TrD) and Junctin (JnC), two proteins that form, with CASQ2 and RyR2, a macromolecular complex devoted to control of calcium release from the sarcoplasmic reticulum. - Source: PubMed
Publication date: 2012/01/31
Denegri MarcoAvelino-Cruz José EverardoBoncompagni SimonaDe Simone Stefano AndreaAuricchio AlbertoVillani LauraVolpe PompeoProtasi FelicianoNapolitano CarloPriori Silvia Giuliana - It is now well documented that human embryonic stem cells (hESCs) can differentiate into functional cardiomyocytes. These cells constitute a promising source of material for use in drug development, toxicity testing, and regenerative medicine. To assess their utility as replacement or complement to existing models, extensive phenotypic characterization of the cells is required. In the present study, we used microarrays and analyzed the global transcription of hESC-derived cardiomyocyte clusters (CMCs) and determined similarities as well as differences compared with reference samples from fetal and adult heart tissue. In addition, we performed a focused analysis of the expression of cardiac ion channels and genes involved in the Ca(2+)-handling machinery, which in previous studies have been shown to be immature in stem cell-derived cardiomyocytes. Our results show that hESC-derived CMCs, on a global level, have a highly similar gene expression profile compared with human heart tissue, and their transcriptional phenotype was more similar to fetal than to adult heart. Despite the high similarity to heart tissue, a number of significantly differentially expressed genes were identified, providing some clues toward understanding the molecular difference between in vivo sourced tissue and stem cell derivatives generated in vitro. Interestingly, some of the cardiac-related ion channels and Ca(2+)-handling genes showed differential expression between the CMCs and heart tissues. These genes may represent candidates for future genetic engineering to create hESC-derived CMCs that better mimic the phenotype of the cardiomyocytes present in the adult human heart. - Source: PubMed
Publication date: 2011/12/13
Synnergren JaneAméen CarolineJansson AndreasSartipy Peter - Calsequestrin (CSQ), the major intrasarcoplasmic reticulum calcium storage protein, undergoes dynamic polymerization and depolymerization in a Ca(2+)-dependent manner. However, no direct evidence of CSQ depolymerization in vivo with physiological relevance has been obtained. In the present study, live cell imaging analysis facilitated characterization of the in vivo dynamics of the macromolecular CSQ structure. CSQ2 appeared as speckles in the presence of normal sarcoplasmic reticulum (SR) Ca(2+) that were decondensed upon Ca(2+) depletion. Moreover, CSQ2 decondensation occurred only in the stoichiometric presence of junctin (JNT). When expressed alone, CSQ2 speckles remained unchanged, even after Ca(2+) depletion. FRET analysis revealed constant interactions between CSQ2 and JNT, regardless of the SR Ca(2+) concentration, implying that JNT is an essential component of the CSQ scaffold. In vitro solubility assay, electron microscopy, and atomic force microscopy studies using purified recombinant proteins confirmed Ca(2+) and JNT-dependent disassembly of the CSQ2 polymer. Accordingly, we conclude that reversible polymerization and depolymerization of CSQ are critical in SR Ca(2+) homeostasis. - Source: PubMed
Publication date: 2011/11/28
Lee Keun WooMaeng Jin-SooChoi Jeong YiLee Yu RanHwang Chae YoungPark Sung SupPark Hyun KyuChung Bong HyunLee Seung-GooKim Yeon-SooJeon HyesungEom Soo HyunKang ChulheeKim Do HanKwon Ki-Sun